Abstract
"Cross-priming" describes the activation of naïve CD8+ T cells by professional antigen-presenting cells that have acquired viral or tumor antigens from "donor" cells. Antigen transfer is believed to be mediated by donor cell-derived molecular chaperones bearing short peptide ligands generated by proteasome degradation of protein antigens. We show here that cross-priming is based on the transfer of proteasome substrates rather than peptides. These findings are potentially important for the rational design of vaccines that elicit CD8+ T cell responses.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Acetylcysteine / analogs & derivatives*
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Acetylcysteine / pharmacology
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Animals
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Antigen Presentation*
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Antigens / immunology*
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Antigens / metabolism
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Antigens, Viral / immunology
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Antigens, Viral / metabolism
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CD8-Positive T-Lymphocytes / immunology*
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Cell Line
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Cross-Priming*
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Cysteine Endopeptidases / metabolism*
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Cysteine Proteinase Inhibitors / pharmacology
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Endoplasmic Reticulum / metabolism
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Humans
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Immunization
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Influenza A virus / immunology
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Lymphocyte Activation
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Mice
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Mice, Inbred C57BL
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Mice, Transgenic
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Molecular Chaperones / metabolism
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Multienzyme Complexes / metabolism*
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Ovalbumin / immunology
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Ovalbumin / metabolism
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Peptide Fragments / immunology
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Proteasome Endopeptidase Complex
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Recombinant Fusion Proteins / immunology
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Recombinant Fusion Proteins / metabolism
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Vaccines / immunology
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Vaccinia virus / genetics
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Vaccinia virus / physiology
Substances
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Antigens
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Antigens, Viral
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Cysteine Proteinase Inhibitors
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Molecular Chaperones
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Multienzyme Complexes
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Peptide Fragments
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Recombinant Fusion Proteins
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Vaccines
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lactacystin
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Ovalbumin
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex
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Acetylcysteine